Release Time:2019-03-09  Hits:

Indexed by: Journal Article

Date of Publication: 2012-06-01

Journal: BIOTECHNOLOGY LETTERS

Included Journals: PubMed、EI、SCIE

Volume: 34

Issue: 6

Page Number: 1107-1113

ISSN: 0141-5492

Key Words: C-C bond hydrolase; Esterase; Homology modeling; Molecular docking

Abstract: A C-C hydrolase gene (bphD (LA-4) ) from strain Dyella ginsengisoli LA-4 was cloned and expressed in Escherichia coli BL21 (DE3). BphD(LA-4) together with another hydrolase MfphA(LA-4), which derived from the same strain, possessed esterase activities. p-Nitrophenyl butyrate was the best substrate for both enzymes. BphD(LA-4) had high catalytic efficiency to p-nitrophenyl benzoate, whereas MfphA(LA-4) had no activity. Homology modeling and docking studies demonstrated that the proper hydrogen bond interaction was important for the reactivity of specific substrate.